ID   A0A0F9ZJH6_9BACT        Unreviewed;       305 AA.
AC   A0A0F9ZJH6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 21.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=UR30_C0013G0025 {ECO:0000313|EMBL:KKP39001.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP39001.1, ECO:0000313|Proteomes:UP000034765};
RN   [1] {ECO:0000313|EMBL:KKP39001.1, ECO:0000313|Proteomes:UP000034765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC       yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC         rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62830; EC=1.1.1.133;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|RuleBase:RU364082}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKP39001.1}.
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DR   EMBL; LBOR01000013; KKP39001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9ZJH6; -.
DR   STRING; 1619061.UR30_C0013G0025; -.
DR   Proteomes; UP000034765; Unassembled WGS sequence.
DR   GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:RHEA.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR   PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT   DOMAIN          6..276
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   305 AA;  35221 MW;  50F220AE0C9EC839 CRC64;
     MKKKSLLILG QGQLGNFYHE YFQEKYQIHF PRIDITKEDQ IKKTIKKYKP QTVINAAAKT
     NIDWCEKNKL QSFEINTLGA DNIGKICEEQ GIYLVHLSSG CIQESKTAKE VKKETDQVHP
     LCFYAWTKVW AEELLMDRKE FGKLKVLILR PRQLLSAKAS PRNAITKMLT YNRFIDTPNS
     CTIIEDLMEA TEHLIRKKAL GIYNIANPGI SSPFKIAKLI QKIVDQDMEV KKISKQELNK
     MTLAKRIDCV LDTTKLKKAG INLHSMEKRL PEILLQFKKN ISTPQGQKIL TKTQEETRKK
     MLVQN
//